scholarly journals A partial proteome reference map of the wine lactic acid bacterium Oenococcus oeni ATCC BAA-1163

Open Biology ◽  
2014 ◽  
Vol 4 (2) ◽  
pp. 130154 ◽  
Author(s):  
María de la Luz Mohedano ◽  
Pasquale Russo ◽  
Vivian de los Ríos ◽  
Vittorio Capozzi ◽  
Pilar Fernández de Palencia ◽  
...  

Oenococcus oeni is the main lactic acid bacterium that carries out the malolactic fermentation in virtually all red wines and in some white and sparkling wines. Oenococcus oeni possesses an array of metabolic activities that can modify the taste and aromatic properties of wine. There is, therefore, industrial interest in the proteins involved in these metabolic pathways and related transport systems of this bacterium. In this work, we report the characterization of the O. oeni ATCC BAA-1163 proteome. Total and membrane protein preparations from O. oeni were standardized and analysed by two-dimensional gel electrophoresis. Using tandem mass spectrometry, we identified 224 different spots corresponding to 152 unique proteins, which have been classified by their putative function and subjected to bioinformatics analysis.

2016 ◽  
Vol 54 ◽  
pp. 167-177 ◽  
Author(s):  
Fety Jaomanjaka ◽  
Olivier Claisse ◽  
Mélanie Blanche-Barbat ◽  
Melina Petrel ◽  
Patricia Ballestra ◽  
...  

2021 ◽  
Vol 11 ◽  
Author(s):  
Cécile Philippe ◽  
Amel Chaïb ◽  
Fety Jaomanjaka ◽  
Olivier Claisse ◽  
Patrick M. Lucas ◽  
...  

There has been little exploration of how phages contribute to the diversity of the bacterial community associated with winemaking and may impact fermentations and product quality. Prophages of Oenococcus oeni, the most common species of lactic acid bacteria (LAB) associated with malolactic fermentation of wine, have been described, but no data is available regarding phages of O. oeni with true virulent lifestyles. The current study reports on the incidence and characterization of the first group of virulent oenophages named Vinitor, isolated from the enological environment. Vinitor phages are morphologically very similar to siphoviruses infecting other LAB. Although widespread during winemaking, they are more abundant in musts than temperate oenophages. We obtained the complete genomic sequences of phages Vinitor162 and Vinitor27, isolated from white and red wines, respectively. The assembled genomes shared 97.6% nucleotide identity and belong to the same species. Coupled with phylogenetic analysis, our study revealed that the genomes of Vinitor phages are architecturally mosaics and represent unique combinations of modules amongst LAB infecting-phages. Our data also provide some clues to possible evolutionary connections between Vinitor and (pro)phages associated to epiphytic and insect-related bacteria.


2009 ◽  
Vol 75 (21) ◽  
pp. 6729-6735 ◽  
Author(s):  
Krista M. Sumby ◽  
Angela H. Matthews ◽  
Paul R. Grbin ◽  
Vladimir Jiranek

ABSTRACT We report the cloning and characterization of EstB28, the first esterase to be so characterized from the wine-associated lactic acid bacterium, Oenococcus oeni. The published sequence for O. oeni strain PSU-1 was used to identify putative esterase genes and design PCR primers in order to amplify the corresponding region from strain Ooeni28, an isolate intended for inoculation of wines. In this way a 912-bp open reading frame (ORF) encoding a putative esterase of 34.5 kDa was obtained. The amino acid sequence indicated that EstB28 is a member of family IV of lipolytic enzymes and contains the GDSAG motif common to other lactic acid bacteria. This ORF was cloned into Escherichia coli using an appropriate expression system, and the recombinant esterase was purified. Characterization of EstB28 revealed that the optimum temperature, pH, and ethanol concentration were 40°C, pH 5.0, and 28% (vol/vol), respectively. EstB28 also retained marked activity under conditions relevant to winemaking (10 to 20°C, pH 3.5, 14% [vol/vol] ethanol). Kinetic constants were determined for EstB28 with p-nitrophenyl (pNP)-linked substrates ranging in chain length from C2 to C18. EstB28 exhibited greatest specificity for C2 to C4 pNP-linked substrates.


2011 ◽  
Vol 74 (8) ◽  
pp. 1309-1314 ◽  
Author(s):  
MARYSE BONNIN-JUSSERAND ◽  
COSETTE GRANDVALET ◽  
VANESSA DAVID ◽  
HERVÉ ALEXANDRE

Ornithine decarboxylase (ODC) is responsible for the production of putrescine, the major biogenic amine found in wine. Oenococcus oeni is the most important lactic acid bacterium in the winemaking process and is involved in malolactic fermentation. We report here the characterization of ODC from an O. oeni strain isolated from wine. Screening of 263 strains isolated from wine and cider from all over the world revealed that the presence of the odc gene appears to be strain specific in O. oeni. After cloning, heterologous expression in Escherichia coli, and characterization, the enzyme was found to have a molecular mass of 85 kDa and a pI of 6.2 and revealed maximal activity at pH 5.5 and an optimum temperature of 35°C. Kinetic studies showed that O. oeni ODC is specific for l-ornithine with a Km value of 1 mM and a Vmax of 0.57 U·mg−1. The hypothesis that cadaverine, which results from lysine decarboxylation, may be linked to putrescine production is not valid since O. oeni ODC cannot decarboxylate L-lysine. As no lysine decarboxylase was detected in any of the O. oeni genomes sequenced, cadaverine synthesis may result from another metabolic pathway. This work is the first characterization of an ODC from a lactic acid bacterium isolated from a fermented product.


2013 ◽  
Vol 11 (4) ◽  
pp. 181-186 ◽  
Author(s):  
Yun-Seok Lee ◽  
Tae-Young Song ◽  
Won-Sik Kong ◽  
Min-Ho Yoon

Author(s):  
Cristobal A. Onetto ◽  
Peter J. Costello ◽  
Radka Kolouchova ◽  
Charlotte Jordans ◽  
Jane McCarthy ◽  
...  

Malolactic fermentation is an indispensable step in the elaboration of most wines and is generally performed by Oenococcus oeni , a Gram-positive heterofermentative lactic acid bacterium species. While O. oeni is tolerant to many of the wine stresses, including low pH and high ethanol concentrations, it has high sensitivity to SO 2 , an antiseptic and antioxidant compound regularly used in winemaking.


2019 ◽  
Vol 64 (1) ◽  
pp. 71-78 ◽  
Author(s):  
Mohamed G. Shehata ◽  
Ahmed N. Badr ◽  
Sobhy A. El Sohaimy ◽  
Dalal Asker ◽  
Tarek S. Awad

2006 ◽  
Vol 401 (2) ◽  
pp. 365-375 ◽  
Author(s):  
Wouter F. Visser ◽  
Carlo W. T. van Roermund ◽  
Lodewijk Ijlst ◽  
Hans R. Waterham ◽  
Ronald J. A. Wanders

In recent years, much progress has been made with respect to the unravelling of the functions of peroxisomes in metabolism, and it is now well established that peroxisomes are indispensable organelles, especially in higher eukaryotes. Peroxisomes catalyse a number of essential metabolic functions including fatty acid β-oxidation, ether phospholipid biosynthesis, fatty acid α-oxidation and glyoxylate detoxification. The involvement of peroxisomes in these metabolic pathways necessitates the transport of metabolites in and out of peroxisomes. Recently, considerable progress has been made in the characterization of metabolite transport across the peroxisomal membrane. Peroxisomes posses several specialized transport systems to transport metabolites. This is exemplified by the identification of a specific transporter for adenine nucleotides and several half-ABC (ATP-binding cassette) transporters which may be present as hetero- and homo-dimers. The nature of the substrates handled by the different ABC transporters is less clear. In this review we will describe the current state of knowledge of the permeability properties of the peroxisomal membrane.


2015 ◽  
Vol 82 (1) ◽  
pp. 18-26 ◽  
Author(s):  
Maud Darsonval ◽  
Tarek Msadek ◽  
Hervé Alexandre ◽  
Cosette Grandvalet

ABSTRACTOenococcus oeniis a wine-associated lactic acid bacterium mostly responsible for malolactic fermentation in wine. In wine,O. oenigrows in an environment hostile to bacterial growth (low pH, low temperature, and ethanol) that induces stress response mechanisms. To survive,O. oeniis known to set up transitional stress response mechanisms through the synthesis of heat stress proteins (HSPs) encoded by thehspgenes, notably a unique small HSP named Lo18. Despite the availability of the genome sequence, characterization ofO. oenigenes is limited, and little is known about thein vivorole of Lo18. Due to the lack of genetic tools forO. oeni, an efficient expression vector inO. oeniis still lacking, and deletion or inactivation of thehsp18gene is not presently practicable. As an alternative approach, with the goal of understanding the biological function of theO. oenihsp18genein vivo, we have developed an expression vector to produce antisense RNA targeting ofhsp18mRNA. Recombinant strains were exposed to multiple stresses inducinghsp18gene expression: heat shock and acid shock. We showed that antisense attenuation ofhsp18affectsO. oenisurvival under stress conditions. These results confirm the involvement of Lo18 in heat and acid tolerance ofO. oeni. Results of anisotropy experiments also confirm a membrane-protective role for Lo18, as previous observations had already suggested. This study describes a new, efficient tool to demonstrate the use of antisense technology for modulating gene expression inO. oeni.


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